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  • 1970-1974  (5)
  • Circular Dichroism  (2)
  • General Chemistry  (2)
  • DNA-Schaden  (1)
  • 1
    ISSN: 1432-1440
    Keywords: Deoxyribonucleases ; diagnosis ; DNA-damage ; microdiscelectrophoresis ; repairmechanism ; urine ; Xeroderma pigmentosum ; Desoxyribonucleasen ; Diagnose ; DNA-Schaden ; Microdiscelektrophorese ; Repairmechanismus ; Urin ; Xeroderma pigmentosum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Das Verteilungsmuster der DNase-Aktivität1 im Urin von Normalpersonen und X.p.-Patienten wurde mit einem mikro-disk-elektrophoretischen Verfahren untersucht. Bei saurer Inkubation sind 4 distinkte Aktivitätsbanden im Normalurin nachweisbar. Urin von X.p.-Patienten zeigt eine deutliche Verminderung der 2.–4. Bande, wobei die Veränderung der 3. Bande besonders auffällig ist. Es wurde ferner untersucht, wie sich das Verhalten verändert, wenn statt nativer DNA denaturierte als Substrat angeboten und wenn die zweiwertigen Ionen durch EDTA komplexiert wurden. Eine Aktivitätsverminderung ist nicht auf das Auftreten von Inhibitoren zurückzuführen, sondern wahrscheinlich durch eine Konzentrationsverminderung an Enzym verursacht.
    Notes: Summary The distribution pattern of desoxyribonuclease (DNase) activity1 in the urine of healthy subjects and xeroderma pigmentosum (X.p.) patients has been examined by micro disc electrophoresis. When incubated at pH 5.0, four distinct bands of DNase activity are shown in normal urine. In urine of X.p. patients a significant decrease of the second to fourth band can be observed. The change of the third band is extremely obvious. Further to the influence of native DNA, denaturated DNA and EDTA on the pattern of DNase activities were studied. The decrease of DNase activity in X. p. urine is not due to the presence of an inhibitor but is rather caused by lower enzyme concentrations.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 278 (1973), S. 301-312 
    ISSN: 1432-1912
    Keywords: Circular Dichroism ; Benzodiazepines ; Albumin-Binding ; Partition Coefficients
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The circular dichroism spectra of 12 benzodiazepine derivatives studied in presence of human serum albumin are presented. Nearly all substances give biphasic extrinsic Cotton effects. At the CD maxima the molar ellipticities and the anisotropy factors are calculated. The influence of the chemical structure of the benzodiazepines on the induced Cotton effect is discussed. There is a linear correlation between the anisotropy factors and the logarithms of the partition coefficients of the substances. It is suggested that the phenyl ring of the benzodiazepine molecule is one of the essential groups for the binding of these substances to human serum albumin.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 283 (1974), S. 67-82 
    ISSN: 1432-1912
    Keywords: Benzodiazepines ; Albumin Binding ; Circular Dichroism ; Gel Filtration ; pH Dependence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The influence of pH on the binding of benzodiazepine derivatives to HSA was studied by circular dichroism measurements and by gel filtration. The binding of nearly all benzodiazepines is increased by rising the pH from 6.60 to 8.20. For flurazepam, clonazepam, and nitrazepam this increase in binding is due to an increase of the affinities, while for the other substances the affinity remains constant and the number of binding sites is increased from one to two. The changes in binding of the benzodiazepines by rising the pH are explained by a cationic amino acid residue near or at the benzodiazepine binding site of the HSA molecule. This second binding site is not detectable by circular dichroism. For several of the substances rising the pH from 6.60 to 8.20, is accompanied by large alterations of the optical properties of the HSA-benzodiazepine complexes. These alterations are explained by changes of the asymmetric environment of the benzodiazepine binding site at the HSA molecule in the structural transition at slightly alkaline pH values. To explain the different reactions of the benzodiazepines within the N→B transition a theory is given.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 83 (1971), S. 766-766 
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 10 (1971), S. 727-728 
    ISSN: 0570-0833
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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